메뉴 건너뛰기




Volumn 54, Issue 6, 2002, Pages 323-333

The role of troponins in muscle contraction

Author keywords

Myopathies; Striated muscle regulation; Troponin isoforms

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; CALCIUM ION; MYOSIN; TROPOMYOSIN; TROPONIN; TROPONIN C; TROPONIN I; TROPONIN T;

EID: 0036926568     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/15216540216037     Document Type: Review
Times cited : (156)

References (85)
  • 1
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman, L. S. (1996) Thin filament-mediated regulation of cardiac contraction. Anuu. Rev. Physiol. 58, 447-481.
    • (1996) Anuu. Rev. Physiol. , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 2
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A. M., Homsher, E., and Regnier, M. (2000) Regulation of contraction in striated muscle. Physiol. Rev. 80, 853-924.
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 4
    • 0037188485 scopus 로고    scopus 로고
    • The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site
    • Li, Y., Mui, S., Brown, J. H., Strand, J., Reshetnikova, L., Tobacman, L. S., and Cohen, C. (2002) The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site. Proc. Natl. Acad. Sci. U.S.A. 99, 7378-7383.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 7378-7383
    • Li, Y.1    Mui, S.2    Brown, J.H.3    Strand, J.4    Reshetnikova, L.5    Tobacman, L.S.6    Cohen, C.7
  • 5
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves, M. A., and Holmes, K. C. (1999) Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68, 687-728.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 6
    • 0034308409 scopus 로고    scopus 로고
    • Cross-bridge action: Present views, prospects, and unknowns
    • Huxley, A. F. (2000) Cross-bridge action: present views, prospects, and unknowns. J. Biomechan. 33, 1189-1195.
    • (2000) J. Biomechan. , vol.33 , pp. 1189-1195
    • Huxley, A.F.1
  • 7
    • 0033579814 scopus 로고    scopus 로고
    • Cooperativity and switching within the three-state model of muscle regulation
    • Maytum, R., Lehrer, S. S., and Geeves, M. A. (1999) Cooperativity and switching within the three-state model of muscle regulation. Biochemistry 38, 1102-1110.
    • (1999) Biochemistry , vol.38 , pp. 1102-1110
    • Maytum, R.1    Lehrer, S.S.2    Geeves, M.A.3
  • 8
    • 0035979730 scopus 로고    scopus 로고
    • Crossbridge and tropomyosin positions observed in native, interacting thick and thin filaments
    • Craig, R., and Lehman, W. (2001) Crossbridge and tropomyosin positions observed in native, interacting thick and thin filaments. J. Mol. Biol. 311, 1027-1036.
    • (2001) J. Mol. Biol. , vol.311 , pp. 1027-1036
    • Craig, R.1    Lehman, W.2
  • 10
    • 0023091230 scopus 로고
    • Structure of co-crystals of tropomyosin and troponin
    • White, S. P., Cohen, C., and Phillips, G. N., Jr. (1987) Structure of co-crystals of tropomyosin and troponin. Nature 325, 826-828.
    • (1987) Nature , vol.325 , pp. 826-828
    • White, S.P.1    Cohen, C.2    Phillips G.N., Jr.3
  • 11
    • 0031855272 scopus 로고    scopus 로고
    • Troponin T: Genetics, properties and function
    • Perry, S. V. (1998) Troponin T: genetics, properties and function. J. Muscle Res. Cell Motil. 19, 575-602.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 575-602
    • Perry, S.V.1
  • 12
    • 0018873792 scopus 로고
    • Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene
    • Wilkinson, J. M. (1980) Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene. Eur. J. Biochem. 103, 179-188.
    • (1980) Eur. J. Biochem. , vol.103 , pp. 179-188
    • Wilkinson, J.M.1
  • 13
    • 0022931544 scopus 로고
    • 2+-induced conformational transition of troponin C. A trigger for muscle contraction
    • 2+-induced conformational transition of troponin C. A trigger for muscle contraction. J. Biol. Chem. 261, 2638-2644.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2638-2644
    • Herzberg, O.1    Moult, J.2    James, M.N.3
  • 15
    • 18844478967 scopus 로고    scopus 로고
    • Backbone and methyl dynamics of the regulatory domain of troponin C: Anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity
    • Gagné, S. M., Tsuda, S., Spyracopoulos, L., Kay, L. E., and Sykes, B. D. (1998) Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity. J. Mol. Biol. 278, 667-686.
    • (1998) J. Mol. Biol. , vol.278 , pp. 667-686
    • Gagné, S.M.1    Tsuda, S.2    Spyracopoulos, L.3    Kay, L.E.4    Sykes, B.D.5
  • 16
    • 0018816959 scopus 로고
    • Structure and evolution of calcium-modulated proteins
    • Kretsinger, R. H. (1980) Structure and evolution of calcium-modulated proteins. CRC Crit. Rev. Biochem. 8, 119-174.
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 119-174
    • Kretsinger, R.H.1
  • 17
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Potter, J. D., and Gergely, J. (1975) The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250, 4628-4633.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4628-4633
    • Potter, J.D.1    Gergely, J.2
  • 18
    • 0023645610 scopus 로고
    • 2+-specific regulatory sites in skinned rabbit psoas fibers
    • 2+-specific regulatory sites in skinned rabbit psoas fibers. J. Biol. Chem. 262, 13627-13635.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13627-13635
    • Guth, K.1    Potter, J.D.2
  • 19
    • 0033383559 scopus 로고    scopus 로고
    • Troponin C regulates the rate constant for the dissociation of force-generating myosin cross-bridges in cardiac muscle
    • Wang, Y., Xu, Y., Guth, K., and Kerrick, W. G. (1999) Troponin C regulates the rate constant for the dissociation of force-generating myosin cross-bridges in cardiac muscle. J. Muscle Res. Cell Motil. 20, 645-653.
    • (1999) J. Muscle Res. Cell Motil. , vol.20 , pp. 645-653
    • Wang, Y.1    Xu, Y.2    Guth, K.3    Kerrick, W.G.4
  • 20
    • 0036088350 scopus 로고    scopus 로고
    • 2+ from troponin C is regulated by force-generating cross bridges in skeletal muscle
    • 2+ from troponin C is regulated by force-generating cross bridges in skeletal muscle. J. Appl. Physiol. 92, 2409-2418.
    • (2002) J. Appl. Physiol. , vol.92 , pp. 2409-2418
    • Wang, Y.1    Kerrick, W.G.L.2
  • 22
    • 0032589143 scopus 로고    scopus 로고
    • 2+ and cross-bridge-induced changes in troponin C in skinned skeletal muscle fibers: Effects of force inhibition
    • 2+ and cross-bridge-induced changes in troponin C in skinned skeletal muscle fibers: effects of force inhibition. Biophys. J. 76, 1480-1493.
    • (1999) Biophys. J. , vol.76 , pp. 1480-1493
    • Martyn, D.A.1    Freitag, C.J.2    Chase, P.B.3    Gordon, A.M.4
  • 23
    • 0028153580 scopus 로고
    • 2+-sensitivity and cooperativity of the tension development in rabbit skeletal and cardiac muscles
    • 2+-sensitivity and cooperativity of the tension development in rabbit skeletal and cardiac muscles. J. Biochem. (Tokyo) 115, 144-146.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 144-146
    • Morimoto, S.1    Ohtsuki, I.2
  • 24
    • 0035827552 scopus 로고    scopus 로고
    • Modulation of contractile activation in skeletal muscle by a calcium-insensitive troponin C Mutant
    • Morris, C. A., Tobacman, L. S., and Homsher, E. (2001) Modulation of contractile activation in skeletal muscle by a calcium-insensitive troponin C Mutant. J. Biol. Chem. 276, 20245-20251.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20245-20251
    • Morris, C.A.1    Tobacman, L.S.2    Homsher, E.3
  • 25
    • 0020000247 scopus 로고
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils. J. Biol. Chem. 257, 7678-7683.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7678-7683
    • Zot, H.G.1    Potter, J.D.2
  • 28
    • 0031576345 scopus 로고    scopus 로고
    • Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 Å resolution
    • Strynadka, N. C., Chemey, M., Sielecki, A. R., Li, M. X., Smillie, L. B., and James, M. N. (1997) Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 Å. resolution. J. Mol. Biol. 273, 238-255.
    • (1997) J. Mol. Biol. , vol.273 , pp. 238-255
    • Strynadka, N.C.1    Chemey, M.2    Sielecki, A.R.3    Li, M.X.4    Smillie, L.B.5    James, M.N.6
  • 29
    • 0030746857 scopus 로고    scopus 로고
    • Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain
    • Sia, S. K., Li, M. X., Spyracopoulos, L., Gagné, S. M., Liu, W., Putkey, J. A., and Sykes, B. D. (1997) Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain. J. Biol. Chem. 272, 18216-18221.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18216-18221
    • Sia, S.K.1    Li, M.X.2    Spyracopoulos, L.3    Gagné, S.M.4    Liu, W.5    Putkey, J.A.6    Sykes, B.D.7
  • 30
    • 0030856717 scopus 로고    scopus 로고
    • Calcium-induced structural transition in the regulatory domain of human cardiac troponin C
    • Spyracopoulos, L., Li, M. X., Sia, S. K., Gagné, S. M., Chandra, M., Solaro, R. J., and Sykes, B. D. (1997) Calcium-induced structural transition in the regulatory domain of human cardiac troponin C. Biochemistry 36, 12138-12146.
    • (1997) Biochemistry , vol.36 , pp. 12138-12146
    • Spyracopoulos, L.1    Li, M.X.2    Sia, S.K.3    Gagné, S.M.4    Chandra, M.5    Solaro, R.J.6    Sykes, B.D.7
  • 31
    • 0034625062 scopus 로고    scopus 로고
    • Bepridil opens the regulatory N-terminal lobe of cardiac troponin C
    • Li, Y., Love, M. L., Putkey, J. A., and Cohen, C. (2000) Bepridil opens the regulatory N-terminal lobe of cardiac troponin C. Proc. Natl. Acad. Sci. U.S.A. 97, 5140-5145.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5140-5145
    • Li, Y.1    Love, M.L.2    Putkey, J.A.3    Cohen, C.4
  • 32
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah, C. S., and Reinach, F. C. (1995) The troponin complex and regulation of muscle contraction. FASEB J. 9, 755-767.
    • (1995) FASEB J. , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 35
    • 0032574791 scopus 로고    scopus 로고
    • Crystal structure of troponin C in complex with troponin I fragment at 2.3-Å resolution
    • Vassylyev, D. G., Takeda, S., Wakatsuki, S., Maeda, K., and Maéda, Y. (1998) Crystal structure of troponin C in complex with troponin I fragment at 2.3-Å resolution. Proc. Natl. Acad. Sci. U.S.A. 95, 4847-4852.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 4847-4852
    • Vassylyev, D.G.1    Takeda, S.2    Wakatsuki, S.3    Maeda, K.4    Maéda, Y.5
  • 38
    • 0033044797 scopus 로고    scopus 로고
    • Troponin I: Inhibitor or facilitator
    • Perry, S. V. (1999) Troponin I: inhibitor or facilitator. Mol. Cell Biochem. 190, 9-32.
    • (1999) Mol. Cell Biochem. , vol.190 , pp. 9-32
    • Perry, S.V.1
  • 39
    • 0032870933 scopus 로고    scopus 로고
    • 2- and COOH-terminal domains of the inhibitory region of troponin I in the regulation of skeletal muscle contraction
    • 2- and COOH-terminal domains of the inhibitory region of troponin I in the regulation of skeletal muscle contraction. J. Biol. Chem. 274, 29536-29542.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29536-29542
    • Szczesna, D.1    Zhang, R.2    Zhao, J.3    Jones, M.4    Potter, J.D.5
  • 41
    • 0036300408 scopus 로고    scopus 로고
    • Troponin-I interacts with the Met47 region of skeletal muscle actin. Implications for the mechanism of thin filament regulation by calcium
    • Luo, Y., Leszyk, J., Li, B., Li, Z., Gergely, J., and Tao, T. (2002) Troponin-I interacts with the Met47 region of skeletal muscle actin. Implications for the mechanism of thin filament regulation by calcium. J. Mol. Biol. 316, 429-434.
    • (2002) J. Mol. Biol. , vol.316 , pp. 429-434
    • Luo, Y.1    Leszyk, J.2    Li, B.3    Li, Z.4    Gergely, J.5    Tao, T.6
  • 42
    • 0034352175 scopus 로고    scopus 로고
    • Integration of cardiac myofilament activity and regulation with pathways signaling hypertrophy and failure
    • de Tombe, P. P., and Solaro, R. J. (2000) Integration of cardiac myofilament activity and regulation with pathways signaling hypertrophy and failure. Ann. Biomed. Eng. 28, 991-1001.
    • (2000) Ann. Biomed. Eng. , vol.28 , pp. 991-1001
    • De Tombe, P.P.1    Solaro, R.J.2
  • 43
    • 0029037870 scopus 로고
    • Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation
    • Zhang, R., Zhao, J., Mandveno, A., and Potter, J. D. (1995) Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation. Circ. Res. 76, 1028-1035.
    • (1995) Circ. Res. , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Mandveno, A.3    Potter, J.D.4
  • 44
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle
    • Kentish, J. C., McCloskey, D. T., Layland, J., Palmer, S., Leiden, J. M., Martin, A. F., and Solaro, R. J. (2001) Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle. Circ. Res. 88, 1059-1065.
    • (2001) Circ. Res. , vol.88 , pp. 1059-1065
    • Kentish, J.C.1    McCloskey, D.T.2    Layland, J.3    Palmer, S.4    Leiden, J.M.5    Martin, A.F.6    Solaro, R.J.7
  • 46
    • 0033593597 scopus 로고    scopus 로고
    • Cardiac troponin I gene knockout: A mouse model of myocardial troponin I deficiency
    • Huang, X., Pi, Y., Lee, K. J., Henkel, A. S., Gregg, R. G., Powers, P. A., and Walker, J. W. (1999) Cardiac troponin I gene knockout: a mouse model of myocardial troponin I deficiency. Circ. Res. 84, 1-8.
    • (1999) Circ. Res. , vol.84 , pp. 1-8
    • Huang, X.1    Pi, Y.2    Lee, K.J.3    Henkel, A.S.4    Gregg, R.G.5    Powers, P.A.6    Walker, J.W.7
  • 47
    • 0033529695 scopus 로고    scopus 로고
    • Functional analysis of troponin I regulatory domains in the intact myofilament of adult single cardiac myocytes
    • Westfall, M. V., Albayya, F. P., and Metzger, J. M. (1999) Functional analysis of troponin I regulatory domains in the intact myofilament of adult single cardiac myocytes. J. Biol. Chem, 274, 22508-22516.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22508-22516
    • Westfall, M.V.1    Albayya, F.P.2    Metzger, J.M.3
  • 50
    • 0019806420 scopus 로고
    • Comparative studies on the inhibitory region of selected species of troponin-I. The use of synthetic peptide analogs to probe structure-function relationships
    • Talbot, J., and Hodges, R. (1981) Comparative studies on the inhibitory region of selected species of troponin-I. The use of synthetic peptide analogs to probe structure-function relationships. J. Biol. Chem. 256, 12374-12378.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12374-12378
    • Talbot, J.1    Hodges, R.2
  • 51
    • 0023930339 scopus 로고
    • The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin
    • Van Eyk, J. E., and Hodges, R. S. (1988) The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin. J. Biol. Chem. 263, 1726-1732.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1726-1732
    • Van Eyk, J.E.1    Hodges, R.S.2
  • 52
    • 0027411141 scopus 로고
    • Protein kinase C-mediated phosphorylation of troponin I and C-protein in isolated myocardial cells is associated with inhibition of myofibrillar actomyosin MgATPase
    • Venema, R., and Kuo, J. (1993) Protein kinase C-mediated phosphorylation of troponin I and C-protein in isolated myocardial cells is associated with inhibition of myofibrillar actomyosin MgATPase. J. Biol. Chem, 268, 2705-2711.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2705-2711
    • Venema, R.1    Kuo, J.2
  • 53
    • 0025896850 scopus 로고
    • 2+-stimulated actomyosin MgATPase activity
    • 2+-stimulated actomyosin MgATPase activity. J. Biol. Chem. 266, 4974-4978.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4974-4978
    • Noland T., Jr.1    Kuo, J.2
  • 55
    • 0036535119 scopus 로고    scopus 로고
    • Quantitative dynamics of site-specific protein phosphorylation determined using liquid chromatography electrospray ionization mass spectrometry
    • Ruse, C. I., Willard, B., Jin, J. P., Haas, T., Kinter, M., and Bond, M. (2002) Quantitative dynamics of site-specific protein phosphorylation determined using liquid chromatography electrospray ionization mass spectrometry. Anal. Chem. 74, 1658-1664.
    • (2002) Anal. Chem. , vol.74 , pp. 1658-1664
    • Ruse, C.I.1    Willard, B.2    Jin, J.P.3    Haas, T.4    Kinter, M.5    Bond, M.6
  • 56
    • 4244091944 scopus 로고    scopus 로고
    • Novel phosphorylation of Ser 149 in cardiac troponin I (cTnI) by PAK reduces the affinity of cTnI for cardiac troponin C (cTnC)
    • Li, M. X., Wang, X., Buscemi, N., Van Eyk, J. E., and Sykes, B. D. (2002) Novel phosphorylation of Ser 149 in cardiac troponin I (cTnI) by PAK reduces the affinity of cTnI for cardiac troponin C (cTnC). Biophys. J. 82, 389A.
    • (2002) Biophys. J. , vol.82
    • Li, M.X.1    Wang, X.2    Buscemi, N.3    Van Eyk, J.E.4    Sykes, B.D.5
  • 57
    • 0025814551 scopus 로고
    • Contractile proteins in globally "stunned" rabbit myocardium
    • Andres, J., Moczarska, A., Stepkowski, D., and Kakol, I. (1991) Contractile proteins in globally "stunned" rabbit myocardium. Basic Res. Cardiol. 86, 219-226.
    • (1991) Basic Res. Cardiol. , vol.86 , pp. 219-226
    • Andres, J.1    Moczarska, A.2    Stepkowski, D.3    Kakol, I.4
  • 58
    • 0026544468 scopus 로고
    • Alterations in myofibrillar function and protein profiles after complete global ischemia in rat hearts
    • Westfall, M. V., and Solaro, R. J. (1992) Alterations in myofibrillar function and protein profiles after complete global ischemia in rat hearts. Circ. Res. 70, 302-313.
    • (1992) Circ. Res. , vol.70 , pp. 302-313
    • Westfall, M.V.1    Solaro, R.J.2
  • 59
    • 0000104030 scopus 로고    scopus 로고
    • Role of troponin I proteolysis in the pathogenesis of stunned myocardium
    • Gao, W. D., Atar, D., Liu, Y., Perez, N. G., Murphy, A. M., and Marban, E. (1997) Role of troponin I proteolysis in the pathogenesis of stunned myocardium. Circ. Res. 80, 393-399.
    • (1997) Circ. Res. , vol.80 , pp. 393-399
    • Gao, W.D.1    Atar, D.2    Liu, Y.3    Perez, N.G.4    Murphy, A.M.5    Marban, E.6
  • 60
    • 0036549817 scopus 로고    scopus 로고
    • Troponin I proteolysis and myocardial stunning: Now you see it - Now you don't
    • Canty, J. M., and Lee, T. C. (2002) Troponin I proteolysis and myocardial stunning: now you see it - now you don't. J. Mol. Cell Cardiol. 34, 375-377.
    • (2002) J. Mol. Cell Cardiol. , vol.34 , pp. 375-377
    • Canty, J.M.1    Lee, T.C.2
  • 62
    • 0033593637 scopus 로고    scopus 로고
    • Troponin I, stunning, hypertrophy, and failure of the heart
    • Solaro, R. J. (1999) Troponin I, stunning, hypertrophy, and failure of the heart. Circ. Res. 84, 122-124.
    • (1999) Circ. Res. , vol.84 , pp. 122-124
    • Solaro, R.J.1
  • 63
    • 0032477852 scopus 로고    scopus 로고
    • Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: Potential role for coiled coil interaction
    • Stefancsik, R., Jha, P. K., and Sarkar, S. (1998) Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: potential role for coiled coil interaction. Proc. Natl. Acad. Sci. U.S.A. 95, 957-962.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 957-962
    • Stefancsik, R.1    Jha, P.K.2    Sarkar, S.3
  • 64
    • 0023071735 scopus 로고
    • Structural aspects of troponintropomyosin regulation of skeletal muscle contraction
    • Zot, A. S., and Potter, J. D. (1987) Structural aspects of troponintropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Biophys. Chem. 16, 535-559.
    • (1987) Annu. Rev. Biophys. Biophys. Chem. , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2
  • 65
    • 0028864262 scopus 로고
    • Separation and characterization of the two functional regions of troponin involved in muscle thin filament regulation
    • Schaertl, S., Lehrer, S. S., and Geeves, M. A. (1995) Separation and characterization of the two functional regions of troponin involved in muscle thin filament regulation. Biochemistry 34, 15890-15894.
    • (1995) Biochemistry , vol.34 , pp. 15890-15894
    • Schaertl, S.1    Lehrer, S.S.2    Geeves, M.A.3
  • 66
    • 0021819912 scopus 로고
    • Intricate combinatorial patterns of exon splicing generate multiple regulated troponin T isoforms from a single gene
    • Breitbart, R. E., Nguyen, H. T., Medford, R. M., Destree, A. T., Mahdavi, V., and Nadal-Ginard, B. (1985) Intricate combinatorial patterns of exon splicing generate multiple regulated troponin T isoforms from a single gene. Cell 41, 67-82.
    • (1985) Cell , vol.41 , pp. 67-82
    • Breitbart, R.E.1    Nguyen, H.T.2    Medford, R.M.3    Destree, A.T.4    Mahdavi, V.5    Nadal-Ginard, B.6
  • 67
    • 0021181932 scopus 로고
    • A novel mechanism of alternative RNA splicing for the developmentally regulated generation of troponin T isoforms from a single gene
    • Medford, R. M., Nguyen, H. T., Destree, A. T., Summers, E., and Nadal-Ginard, B. (1984) A novel mechanism of alternative RNA splicing for the developmentally regulated generation of troponin T isoforms from a single gene. Cell 38, 409-421.
    • (1984) Cell , vol.38 , pp. 409-421
    • Medford, R.M.1    Nguyen, H.T.2    Destree, A.T.3    Summers, E.4    Nadal-Ginard, B.5
  • 68
    • 0022235739 scopus 로고
    • A single cardiac troponin T gene generates embryonic and adult isoforms via developmentally regulated alternate splicing
    • Cooper, T. A., and Ordahl, C. P. (1985) A single cardiac troponin T gene generates embryonic and adult isoforms via developmentally regulated alternate splicing. J. Biol. Chem. 260, 11140-11148.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11140-11148
    • Cooper, T.A.1    Ordahl, C.P.2
  • 70
    • 0025934457 scopus 로고
    • Troponin T isoform expression in humans. A comparison among normal and failing adult heart, fetal heart, and adult and fetal skeletal muscle
    • Anderson, P. A., Malouf, N. N., Oakeley, A. E., Pagani, E. D., and Allen, P. D. (1991) Troponin T isoform expression in humans. A comparison among normal and failing adult heart, fetal heart, and adult and fetal skeletal muscle. Circ. Res. 69, 1226-1233.
    • (1991) Circ. Res. , vol.69 , pp. 1226-1233
    • Anderson, P.A.1    Malouf, N.N.2    Oakeley, A.E.3    Pagani, E.D.4    Allen, P.D.5
  • 71
    • 0037144508 scopus 로고    scopus 로고
    • 2+ sensitivity and inhibition of force development: Insights into the role of troponin T isoforms in the heart
    • 2+ sensitivity and inhibition of force development: insights into the role of troponin T isoforms in the heart. J. Biol. Chem. 277, 35341-35349.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35341-35349
    • Gomes, A.V.1    Guzman, G.2    Zhao, J.3    Potter, J.D.4
  • 72
    • 0037119477 scopus 로고    scopus 로고
    • A modulatory role for the troponin T tail domain in thin filament regulation
    • Maytum, R., Geeves, M. A., and Lehrer, S. S. (2002) A modulatory role for the troponin T tail domain in thin filament regulation. J. Biol. Chem. 277, 29774-29780.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29774-29780
    • Maytum, R.1    Geeves, M.A.2    Lehrer, S.S.3
  • 73
    • 0037008682 scopus 로고    scopus 로고
    • The troponin tail domain promotes a conformational state of the thin filament that suppresses myosin activity
    • Tobacman, L. S., Nihli, M., Butters, C., Heller, M., Hatch, V., Craig, R., Lehman, W., and Homsher, E. (2002) The troponin tail domain promotes a conformational state of the thin filament that suppresses myosin activity. J. Biol. Chem. 277, 27636-27642.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27636-27642
    • Tobacman, L.S.1    Nihli, M.2    Butters, C.3    Heller, M.4    Hatch, V.5    Craig, R.6    Lehman, W.7    Homsher, E.8
  • 74
    • 0029813865 scopus 로고    scopus 로고
    • Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties
    • Jideama, N. M., Noland, T. A., Jr., Raynor, R. L., Blobe, G. C., Fabbro, D., Kazanietz, M. G., Blumberg, P. M., Hannun, Y. A., and Kuo, J. F. (1996) Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties. J. Biol. Chem. 271, 23277-23283.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23277-23283
    • Jideama, N.M.1    Noland T.A., Jr.2    Raynor, R.L.3    Blobe, G.C.4    Fabbro, D.5    Kazanietz, M.G.6    Blumberg, P.M.7    Hannun, Y.A.8    Kuo, J.F.9
  • 75
    • 0026437798 scopus 로고
    • 2+-dependent actomyosin MgATPase activity and troponin T binding to tropomyosin-F-actin complex
    • 2+-dependent actomyosin MgATPase activity and troponin T binding to tropomyosin-F-actin complex. Biochem. J. 288, 123-129.
    • (1992) Biochem. J. , vol.288 , pp. 123-129
    • Noland T.A., Jr.1    Kuo, J.F.2
  • 77
    • 0035109415 scopus 로고    scopus 로고
    • Invited review: Pathophysiology of cardiac muscle contraction and relaxation as a result of alterations in thin filament regulation
    • Hernandez, O. M., Housmans, P. R., and Potter, J. D. (2001) Invited review: pathophysiology of cardiac muscle contraction and relaxation as a result of alterations in thin filament regulation. J. Appl. Physiol. 90, 1125-1136.
    • (2001) J. Appl. Physiol. , vol.90 , pp. 1125-1136
    • Hernandez, O.M.1    Housmans, P.R.2    Potter, J.D.3
  • 78
    • 0034796231 scopus 로고    scopus 로고
    • Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy
    • Knollmann, B. C., and Potter, J. D. (2001) Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy. Trends Cardiovasc. Med. 11, 206-212.
    • (2001) Trends Cardiovasc. Med. , vol.11 , pp. 206-212
    • Knollmann, B.C.1    Potter, J.D.2
  • 80
    • 0033214054 scopus 로고    scopus 로고
    • Functional consequences of troponin T mutations found in hypertrophic cardiomyopathy
    • Tobacman, L. S., Lin, D., Butters, C., Landis, C., Back, N., Pavlov, D., and Homsher, E. (1999) Functional consequences of troponin T mutations found in hypertrophic cardiomyopathy. J. Biol. Chem. 274, 28363-28370.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28363-28370
    • Tobacman, L.S.1    Lin, D.2    Butters, C.3    Landis, C.4    Back, N.5    Pavlov, D.6    Homsher, E.7
  • 84
    • 0035378612 scopus 로고    scopus 로고
    • First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy
    • Hoffmann, B., Schmidt-Traub, H., Perrot, A., Osterziel, K. J., and Gessner, R. (2001) First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy. Hum. Mutat. 17, 524.
    • (2001) Hum. Mutat. , vol.17 , pp. 524
    • Hoffmann, B.1    Schmidt-Traub, H.2    Perrot, A.3    Osterziel, K.J.4    Gessner, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.